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URH1_YEAST
ID   URH1_YEAST              Reviewed;         340 AA.
AC   Q04179; D6VT33;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 2.
DT   03-AUG-2022, entry version 159.
DE   RecName: Full=Uridine nucleosidase;
DE            EC=3.2.2.3;
DE   AltName: Full=Uridine ribohydrolase;
GN   Name=URH1; OrderedLocusNames=YDR400W; ORFNames=D9509.19;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION, IDENTIFICATION OF
RP   PROBABLE INITIATION SITE, AND MUTAGENESIS OF HIS-254.
RX   PubMed=12111094; DOI=10.1007/s00294-002-0296-9;
RA   Kurtz J.-E., Exinger F., Erbs P., Jund R.;
RT   "The URH1 uridine ribohydrolase of Saccharomyces cerevisiae.";
RL   Curr. Genet. 41:132-141(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=237897; DOI=10.1016/s0021-9258(19)41972-8;
RA   Magni G., Fioretti E., Ipata P.L., Natalini P.;
RT   "Bakers' yeast uridine nucleosidase. Purification, composition, and
RT   physical and enzymatic properties.";
RL   J. Biol. Chem. 250:9-13(1975).
RN   [5]
RP   IDENTIFICATION OF PROBABLE INITIATION SITE.
RX   PubMed=12748633; DOI=10.1038/nature01644;
RA   Kellis M., Patterson N., Endrizzi M., Birren B.W., Lander E.S.;
RT   "Sequencing and comparison of yeast species to identify genes and
RT   regulatory elements.";
RL   Nature 423:241-254(2003).
RN   [6]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
CC   -!- FUNCTION: Also acts on cytidine.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + uridine = D-ribose + uracil; Xref=Rhea:RHEA:15577,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16704, ChEBI:CHEBI:17568,
CC         ChEBI:CHEBI:47013; EC=3.2.2.3;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.86 mM for uridine {ECO:0000269|PubMed:237897};
CC         KM=1.66 mM for 5-methyluridine {ECO:0000269|PubMed:237897};
CC       pH dependence:
CC         Optimum pH is 7.0-7.2. {ECO:0000269|PubMed:237897};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus
CC       {ECO:0000269|PubMed:14562095}.
CC   -!- SIMILARITY: Belongs to the IUNH family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB64841.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=AAG44107.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF217406; AAG44107.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U32274; AAB64841.1; ALT_INIT; Genomic_DNA.
DR   EMBL; BK006938; DAA12243.1; -; Genomic_DNA.
DR   PIR; S69683; S69683.
DR   RefSeq; NP_010688.4; NM_001180708.3.
DR   AlphaFoldDB; Q04179; -.
DR   SMR; Q04179; -.
DR   BioGRID; 32461; 66.
DR   DIP; DIP-1845N; -.
DR   IntAct; Q04179; 2.
DR   MINT; Q04179; -.
DR   STRING; 4932.YDR400W; -.
DR   iPTMnet; Q04179; -.
DR   MaxQB; Q04179; -.
DR   PaxDb; Q04179; -.
DR   PRIDE; Q04179; -.
DR   EnsemblFungi; YDR400W_mRNA; YDR400W; YDR400W.
DR   GeneID; 852009; -.
DR   KEGG; sce:YDR400W; -.
DR   SGD; S000002808; URH1.
DR   VEuPathDB; FungiDB:YDR400W; -.
DR   eggNOG; KOG2938; Eukaryota.
DR   HOGENOM; CLU_036838_2_0_1; -.
DR   InParanoid; Q04179; -.
DR   OMA; HAPDIHG; -.
DR   BioCyc; MetaCyc:YDR400W-MON; -.
DR   BioCyc; YEAST:YDR400W-MON; -.
DR   BRENDA; 3.2.2.3; 984.
DR   SABIO-RK; Q04179; -.
DR   PRO; PR:Q04179; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q04179; protein.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0070635; F:nicotinamide riboside hydrolase activity; IDA:SGD.
DR   GO; GO:0070636; F:nicotinic acid riboside hydrolase activity; IDA:SGD.
DR   GO; GO:0008477; F:purine nucleosidase activity; IBA:GO_Central.
DR   GO; GO:0050263; F:ribosylpyrimidine nucleosidase activity; IDA:SGD.
DR   GO; GO:0045437; F:uridine nucleosidase activity; IDA:SGD.
DR   GO; GO:0006216; P:cytidine catabolic process; IMP:SGD.
DR   GO; GO:0034356; P:NAD biosynthesis via nicotinamide riboside salvage pathway; IGI:SGD.
DR   GO; GO:0019358; P:nicotinate nucleotide salvage; IGI:SGD.
DR   GO; GO:0006152; P:purine nucleoside catabolic process; IBA:GO_Central.
DR   GO; GO:0046135; P:pyrimidine nucleoside catabolic process; IDA:SGD.
DR   GO; GO:0008655; P:pyrimidine-containing compound salvage; IMP:SGD.
DR   GO; GO:0006218; P:uridine catabolic process; IMP:SGD.
DR   Gene3D; 3.90.245.10; -; 1.
DR   InterPro; IPR015910; I/U_nuclsd_hydro_CS.
DR   InterPro; IPR001910; Inosine/uridine_hydrolase_dom.
DR   InterPro; IPR023186; IUNH.
DR   InterPro; IPR036452; Ribo_hydro-like.
DR   PANTHER; PTHR12304; PTHR12304; 1.
DR   Pfam; PF01156; IU_nuc_hydro; 1.
DR   SUPFAM; SSF53590; SSF53590; 1.
DR   PROSITE; PS01247; IUNH; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Glycosidase; Hydrolase; Nucleus; Reference proteome.
FT   CHAIN           1..340
FT                   /note="Uridine nucleosidase"
FT                   /id="PRO_0000206812"
FT   ACT_SITE        254
FT                   /evidence="ECO:0000250"
FT   MUTAGEN         254
FT                   /note="H->A: Reduces the Vmax 30-fold, but does not change
FT                   the KM in a uridine hydrolase assay."
FT                   /evidence="ECO:0000269|PubMed:12111094"
SQ   SEQUENCE   340 AA;  37960 MW;  DBFF62F8F1629C74 CRC64;
     MTVSKIPIWL DCDPGHDDAI AILLGCFHPA FNLLGISTCF GNAPPENTDY NARSLLTAMG
     KAQAIPVYKG AQRPWKREPH YAPDIHGISG LDGTSLLPKP TFEARTDKTY IEAIEEAILA
     NNGEISFVST GALTTLATVF RCKPYLKKSV KYISIMGGGL HGLGNCNPNL SAEFNVWIDP
     DAANYIFRDP DVKDKCIVVP LNLTHKAIAT YKVNEMIYNE KNNSKLRELF LELFQFFAHT
     YKDMQGFESG PPIHDPVALM PLLEFYGWDP SSAVGFRYKR MDISCIDDVF NENSGKIIIE
     KEYPNDSDVG TIIGLDLNIQ YFWDQIFEAL NRADKMSTIG
 
 
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